ID A0A2K6SXL0_SAIBB Unreviewed; 950 AA.
AC A0A2K6SXL0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 15 {ECO:0000313|Ensembl:ENSSBOP00000012139.1};
GN Name=ADAMTS15 {ECO:0000313|Ensembl:ENSSBOP00000012139.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000012139.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000012139.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR RefSeq; XP_003923551.1; XM_003923502.2.
DR AlphaFoldDB; A0A2K6SXL0; -.
DR STRING; 39432.ENSSBOP00000012139; -.
DR Ensembl; ENSSBOT00000028928.1; ENSSBOP00000012139.1; ENSSBOG00000022891.1.
DR GeneID; 101029523; -.
DR KEGG; sbq:101029523; -.
DR CTD; 170689; -.
DR GeneTree; ENSGT00940000155801; -.
DR OMA; LARDRCN; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0022617; P:extracellular matrix disassembly; IEA:Ensembl.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013277; Pept_M12B_ADAM-TS8.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF39; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 15; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01861; ADAMTS8.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..950
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014351576"
FT DOMAIN 218..427
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 152..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 362
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 293..345
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 322..327
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 339..422
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..406
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 448..470
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 459..480
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 465..499
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 493..504
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 528..565
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 532..570
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 543..555
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 950 AA; 103423 MW; 4F4B8CB656E26A54 CRC64;
MLLLGILTLA FAGRTAGSSQ PEREVVVPIR LDPDINGRHY YWRGPEDSGD QGLIFQITAF
QEDFYLHLTP DAQFLAPAFA TEHLGVPLQG LARGSSELRR CFYSGDVNAE PDSFAAVSLC
GGLRGAFGYR GAEYVISPLP NASAPAAQRN SQGAHLLQRR GVPGGPSGGP TSRCGVASGW
NPAILRALDP YKPRRASLGE SRSRRRSGRA KRFVSIPRYV ETLVVADESM VKFHGADLEH
YLLTLLATAA RLYRHPSILN PINIVVVKVL LLRDRDSGPK VTGNAALTLR NFCAWQKKLN
KVSDKHPEYW DTAILFTRQD LCGATTCDTL GMADVGTMCD PKRSCSVIED DGLPSAFTTA
HELGHVFNMP HDNVKVCEEV FGKLRANHMM SPTLIQIDRA NPWSACSAAI ITDFLDSGHG
DCLLDQPSKP ISLPEDLPGT SYTLSQQCEL AFGVGSKPCP YMQYCTKLWC TGKAKGQMVC
QTRHFPWADG TSCGDGRFCL KGACVERHNL NKHKVDGSWA KWEPYGPCSR TCGGGVQLAR
RQCTNPTPAN GGKYCEGVRV KYRSCNLEPC PSSASGKSFR EEQCEAFNGY NHSTNRLTLA
VAWVPKYSGV SPRDKCKLIC RANGTGYFYV LAPKVVDGTL CSPDSTSICV QGKCIKAGCD
GNLGSKKRFD KCGVCGGDNK SCKKVTGLFT KPMHGYNFVV AIPAGASSID IRQRGYKGLI
GDDNYLALKN SQGKYLLNGH FVVSAVERDL AVKGSLLRYS GTGTAVESLQ ASRPILEPLT
VEVLSVGKMT PPRVRYSFYL PKEPREDKSS HPKDPRPPSV LHNSVLSLSN QVEQPDHRPP
ARWVAGSWGP CSVSCGSGLQ KRVVDCRGSP GQRAVPACDA AHRPVETQTC GGPCPTWEVS
AWSPCSKSCG RGFKRRPLKC VGHGGRLLAR DQCNPRRKPQ ELDFCVLRPC
//
